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Genome polyprotein [Cleaved into: Protein VP0 (VP4-VP2); Protein VP4 (P1A) (Virion protein 4); Protein VP2 (P1B) (Virion protein 2); Protein VP3 (P1C) (Virion protein 3); Protein VP1-2A (PX); Protein VP1 (P1D) (Virion protein 1); Protein 2A (P2A); Protein 2BC; Protein 2B (P2B); Protein 2C (P2C) (EC 3.6.1.15); Protein 3ABCD (P3); Protein 3ABC; Protein 3AB; Protein 3A (P3A); Protein 3B (P3B) (VPg); Protein 3CD; Protease 3C (P3C) (EC 3.4.22.28) (Picornain 3C); RNA-directed RNA polymerase 3D-POL (P3D-POL) (EC 2.7.7.48)]

 POLG_HAVHM              Reviewed;        2227 AA.
P08617; P06443; P26580; P26581; P26582; Q81082; Q81094; Q8V405;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
12-SEP-2018, entry version 157.
RecName: Full=Genome polyprotein;
Contains:
RecName: Full=Protein VP0;
AltName: Full=VP4-VP2;
Contains:
RecName: Full=Protein VP4;
AltName: Full=P1A;
AltName: Full=Virion protein 4;
Contains:
RecName: Full=Capsid protein VP2;
AltName: Full=P1B;
AltName: Full=Virion protein 2;
Contains:
RecName: Full=Capsid protein VP3;
AltName: Full=P1C;
AltName: Full=Virion protein 3;
Contains:
RecName: Full=Protein VP1-2A;
AltName: Full=VP1-pX;
Contains:
RecName: Full=Capsid protein VP1;
AltName: Full=P1D;
AltName: Full=Virion protein 1;
Contains:
RecName: Full=Assembly signal 2A;
AltName: Full=pX {ECO:0000303|PubMed:23542590};
Contains:
RecName: Full=Protein 2BC;
Contains:
RecName: Full=Protein 2B;
Short=P2B;
Contains:
RecName: Full=Protein 2C;
Short=P2C;
EC=3.6.1.15;
Contains:
RecName: Full=Protein 3ABCD;
Short=P3;
Contains:
RecName: Full=Protein 3ABC;
Contains:
RecName: Full=Protein 3AB;
Contains:
RecName: Full=Protein 3A;
Short=P3A;
Contains:
RecName: Full=Viral protein genome-linked;
Short=VPg;
AltName: Full=Protein 3B;
Short=P3B;
Contains:
RecName: Full=Protein 3CD;
Contains:
RecName: Full=Protease 3C;
Short=P3C;
EC=3.4.22.28 {ECO:0000269|PubMed:1850033};
AltName: Full=Picornain 3C;
Contains:
RecName: Full=RNA-directed RNA polymerase 3D-POL;
Short=P3D-POL;
EC=2.7.7.48 {ECO:0000269|PubMed:8291234};
Human hepatitis A virus genotype IB (isolate HM175) (HHAV) (Human
hepatitis A virus (isolate Human/Australia/HM175/1976)).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Picornavirales; Picornaviridae; Hepatovirus.
NCBI_TaxID=12098;
NCBI_TaxID=9536; Cercopithecus hamlyni (Owl-faced monkey) (Hamlyn's monkey).
NCBI_TaxID=9606; Homo sapiens (Human).
NCBI_TaxID=9539; Macaca (macaques).
NCBI_TaxID=9598; Pan troglodytes (Chimpanzee).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=HM175/wt;
PubMed=3023706;
Cohen J.I., Ticehurst J.R., Purcell R.H., Buckler-White A.,
Baroudy B.M.;
"Complete nucleotide sequence of wild-type hepatitis A virus:
comparison with different strains of hepatitis A virus and other
picornaviruses.";
J. Virol. 61:50-59(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=HM175/7 MK-5;
PubMed=3031686; DOI=10.1073/pnas.84.8.2497;
Cohen J.I., Rosenblum B., Ticehurst J.R., Daemer R.J., Feinstone S.M.,
Purcell R.H.;
"Complete nucleotide sequence of an attenuated hepatitis A virus:
comparison with wild-type virus.";
Proc. Natl. Acad. Sci. U.S.A. 84:2497-2501(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=HM175/18f, HM175/24a, and HM175/43c;
PubMed=1705995;
Lemon S.M., Murphy P.C., Shields P.A., Ping L.H., Feinstone S.M.,
Cromeans T., Jansen R.W.;
"Antigenic and genetic variation in cytopathic hepatitis A virus
variants arising during persistent infection: evidence for genetic
recombination.";
J. Virol. 65:2056-2065(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-854 AND 1724-2227.
PubMed=2984684; DOI=10.1073/pnas.82.7.2143;
Baroudy B.M., Ticehurst J.R., Miele T.A., Maizel J.V. Jr.,
Purcell R.H., Feinstone S.M.;
"Sequence analysis of hepatitis A virus cDNA coding for capsid
proteins and RNA polymerase.";
Proc. Natl. Acad. Sci. U.S.A. 82:2143-2147(1985).
[5]
PROTEIN SEQUENCE OF 837-856, MUTAGENESIS OF GLN-836, AND PROTEOLYTIC
CLEAVAGE (GENOME POLYPROTEIN).
STRAIN=HM175p35;
PubMed=7483265; DOI=10.1006/viro.1995.1561;
Martin A., Escriou N., Chao S.-F., Girard M., Lemon S.M.,
Wychowski C.;
"Identification and site-directed mutagenesis of the primary (2A/2B)
cleavage site of the hepatitis A virus polyprotein: functional impact
on the infectivity of HAV RNA transcripts.";
Virology 213:213-222(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 2090-2227.
PubMed=6310601; DOI=10.1073/pnas.80.19.5885;
Ticehurst J.R., Racaniello V.R., Baroudy B.M., Baltimore D.,
Purcell R.H., Feinstone S.M.;
"Molecular cloning and characterization of hepatitis A virus cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 80:5885-5889(1983).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-819.
STRAIN=Isolate Val8;
PubMed=12409389; DOI=10.1128/JCM.40.11.4148-4155.2002;
Sanchez G., Pinto R.M., Vanaclocha H., Bosch A.;
"Molecular characterization of hepatitis a virus isolates from a
transcontinental shellfish-borne outbreak.";
J. Clin. Microbiol. 40:4148-4155(2002).
[8]
IDENTIFICATION (VIRAL PROTEIN GENOME-LINKED).
PubMed=3018280;
Weitz M., Baroudy B.M., Maloy W.L., Ticehurst J.R., Purcell R.H.;
"Detection of a genome-linked protein (VPg) of hepatitis A virus and
its comparison with other picornaviral VPgs.";
J. Virol. 60:124-130(1986).
[9]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), FUNCTION (PROTEASE 3C), AND
CATALYTIC ACTIVITY (PROTEASE 3C).
PubMed=1850033;
Jia X.-Y., Ehrenfeld E., Summers D.F.;
"Proteolytic activity of hepatitis A virus 3C protein.";
J. Virol. 65:2595-2600(1991).
[10]
IDENTIFICATION OF N-TERMINUS (GENOME POLYPROTEIN).
STRAIN=HM175/7;
PubMed=1310188; DOI=10.1016/0042-6822(92)90027-M;
Tesar M., Harmon S.A., Summers D.F., Ehrenfeld E.;
"Hepatitis A virus polyprotein synthesis initiates from two
alternative AUG codons.";
Virology 186:609-618(1992).
[11]
ABSENCE OF MYRISTOYLATION (PROTEIN VP4).
STRAIN=HM175/7;
PubMed=8389076; DOI=10.1006/viro.1993.1301;
Tesar M., Jia X.-Y., Summers D.F., Ehrenfeld E.;
"Analysis of a potential myristoylation site in hepatitis A virus
capsid protein VP4.";
Virology 194:616-626(1993).
[12]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=8382411; DOI=10.1006/viro.1993.1157;
Jia X.-Y., Summers D.F., Ehrenfeld E.;
"Primary cleavage of the HAV capsid protein precursor in the middle of
the proposed 2A coding region.";
Virology 193:515-519(1993).
[13]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), AND CATALYTIC ACTIVITY
(RNA-DIRECTED RNA POLYMERASE 3D-POL).
PubMed=8291234; DOI=10.1006/viro.1994.1063;
Tesar M., Pak I., Jia X.-Y., Richards O.C., Summers D.F.,
Ehrenfeld E.;
"Expression of hepatitis A virus precursor protein P3 in vivo and in
vitro: polyprotein processing of the 3CD cleavage site.";
Virology 198:524-533(1994).
[14]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=8259663;
Schultheiss T., Kusov Y.Y., Gauss-Mueller V.;
"Proteinase 3C of hepatitis A virus (HAV) cleaves the HAV polyprotein
P2-P3 at all sites including VP1/2A and 2A/2B.";
Virology 198:275-281(1994).
[15]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=7853510;
Schultheiss T., Sommergruber W., Kusov Y., Gauss-Mueller V.;
"Cleavage specificity of purified recombinant hepatitis A virus 3C
proteinase on natural substrates.";
J. Virol. 69:1727-1733(1995).
[16]
FUNCTION (PROTEIN 3AB).
PubMed=7601283;
Lama J., Carrasco L.;
"Mutations in the hydrophobic domain of poliovirus protein 3AB
abrogate its permeabilizing activity.";
FEBS Lett. 367:5-11(1995).
[17]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=9060697;
Probst C., Jecht M., Gauss-Mueller V.;
"Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus
strains: in vivo evidence for cleavage at amino acid position 273/274
of VP1.";
J. Virol. 71:3288-3292(1997).
[18]
FUNCTION (PROTEIN 2C), FUNCTION (PROTEIN 2BC), AND FUNCTION (PROTEIN
2B).
STRAIN=HM175/24a, HM175/wt, and HM175p35;
PubMed=9344908; DOI=10.1006/viro.1997.8775;
Teterina N.L., Bienz K., Egger D., Gorbalenya A.E., Ehrenfeld E.;
"Induction of intracellular membrane rearrangements by HAV proteins 2C
and 2BC.";
Virology 237:66-77(1997).
[19]
SUBUNIT (PROTEIN 3AB), FUNCTION (PROTEIN 3AB), TOPOLOGY (PROTEIN 3AB),
TOPOLOGY (PROTEIN 3A), AND FUNCTION (PROTEIN 3A).
PubMed=9705870; DOI=10.1006/bbrc.1998.9121;
Ciervo A., Beneduce F., Morace G.;
"Polypeptide 3AB of hepatitis A virus is a transmembrane protein.";
Biochem. Biophys. Res. Commun. 249:266-274(1998).
[20]
SUBCELLULAR LOCATION (PROTEIN 2C), RNA-BINDING (PROTEIN 2C), AND
FUNCTION (PROTEIN 2C).
PubMed=9645199; DOI=10.1007/s007050050343;
Kusov Y.Y., Probst C., Jecht M., Jost P.D., Gauss-Mueller V.;
"Membrane association and RNA binding of recombinant hepatitis A virus
protein 2C.";
Arch. Virol. 143:931-944(1998).
[21]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=9733840;
Probst C., Jecht M., Gauss-Mueller V.;
"Processing of proteinase precursors and their effect on hepatitis A
virus particle formation.";
J. Virol. 72:8013-8020(1998).
[22]
FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), AND
FUNCTION (CAPSID PROTEIN VP3).
PubMed=9658108;
Feigelstock D., Thompson P., Mattoo P., Zhang Y., Kaplan G.G.;
"The human homolog of HAVcr-1 codes for a hepatitis A virus cellular
receptor.";
J. Virol. 72:6621-6628(1998).
[23]
FUNCTION (PROTEIN 2B), FUNCTION (PROTEIN 2BC), SUBCELLULAR LOCATION
(PROTEIN 2B), AND SUBCELLULAR LOCATION (PROTEIN 2C).
PubMed=9875331; DOI=10.1006/viro.1998.9451;
Jecht M., Probst C., Gauss-Mueller V.;
"Membrane permeability induced by hepatitis A virus proteins 2B and
2BC and proteolytic processing of HAV 2BC.";
Virology 252:218-227(1998).
[24]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), AND FUNCTION (PROTEIN
3ABC).
PubMed=10559299;
Kusov Y., Gauss-Mueller V.;
"Improving proteolytic cleavage at the 3A/3B site of the hepatitis A
virus polyprotein impairs processing and particle formation, and the
impairment can be complemented in trans by 3AB and 3ABC.";
J. Virol. 73:9867-9878(1999).
[25]
FUNCTION (PROTEIN 3AB), INTERACTION WITH PROTEIN 3CD (PROTEIN 3AB),
INTERACTION WITH PROTEIN 3AB (PROTEIN 3CD), RNA-BINDING (PROTEIN 3AB),
FUNCTION (PROTEIN 3A), AND FUNCTION (PROTEIN 3CD).
STRAIN=HM175/7;
PubMed=10562502; DOI=10.1006/viro.1999.0017;
Beneduce F., Ciervo A., Kusov Y.Y., Gauss-Mueller V., Morace G.;
"Mapping of protein domains of hepatitis A virus 3AB essential for
interaction with 3CD and viral RNA.";
Virology 264:410-421(1999).
[26]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), AND PROTEOLYTIC CLEAVAGE
(PROTEIN VP1-2A).
STRAIN=HM175p35, and HM175pE;
PubMed=10364353;
Graff J., Richards O.C., Swiderek K.M., Davis M.T., Rusnak F.,
Harmon S.A., Jia X.-Y., Summers D.F., Ehrenfeld E.;
"Hepatitis A virus capsid protein VP1 has a heterogeneous C
terminus.";
J. Virol. 73:6015-6023(1999).
[27]
FUNCTION (PROTEIN VP1-2A), AND FUNCTION (PROTEIN VP4).
PubMed=9988685; DOI=10.1074/jbc.274.8.4527;
Probst C., Jecht M., Gauss-Mueller V.;
"Intrinsic signals for the assembly of hepatitis A virus particles.
Role of structural proteins VP4 and 2A.";
J. Biol. Chem. 274:4527-4531(1999).
[28]
FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), AND
FUNCTION (CAPSID PROTEIN VP3).
PubMed=11134285; DOI=10.1128/JVI.75.2.717-725.2001;
Silberstein E., Dveksler G., Kaplan G.G.;
"Neutralization of hepatitis A virus (HAV) by an immunoadhesin
containing the cysteine-rich region of HAV cellular receptor-1.";
J. Virol. 75:717-725(2001).
[29]
FUNCTION (PROTEIN VP1-2A), AND DOMAIN (PROTEIN VP1-2A).
STRAIN=HM175/18f;
PubMed=12097562; DOI=10.1128/JVI.76.15.7495-7505.2002;
Cohen L., Benichou D., Martin A.;
"Analysis of deletion mutants indicates that the 2A polypeptide of
hepatitis A virus participates in virion morphogenesis.";
J. Virol. 76:7495-7505(2002).
[30]
SUBUNIT (PROTEIN VP1-2A), MUTAGENESIS OF ARG-769, DOMAIN (PROTEIN
VP1-2A), AND PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN).
PubMed=12782637; DOI=10.1074/jbc.M300454200;
Rachow A., Gauss-Mueller V., Probst C.;
"Homogenous hepatitis A virus particles. Proteolytic release of the
assembly signal 2A from procapsids by factor Xa.";
J. Biol. Chem. 278:29744-29751(2003).
[31]
MUTAGENESIS OF ALA-1052.
PubMed=12858403; DOI=10.1002/jmv.10457;
Graff J., Emerson S.U.;
"Importance of amino acid 216 in nonstructural protein 2B for
replication of hepatitis A virus in cell culture and in vivo.";
J. Med. Virol. 71:7-17(2003).
[32]
MUTAGENESIS OF CYS-1543 AND CYS-1691, DISULFIDE BOND (PROTEASE 3C),
SUBUNIT (PROTEASE 3C), AND RNA-BINDING (PROTEASE 3C).
PubMed=15361063; DOI=10.1042/BJ20041153;
Peters H., Kusov Y.Y., Meyer S., Benie A.J., Baeuml E., Wolff M.,
Rademacher C., Peters T., Gauss-Mueller V.;
"Hepatitis A virus proteinase 3C binding to viral RNA: correlation
with substrate binding and enzyme dimerization.";
Biochem. J. 385:363-370(2005).
[33]
FUNCTION (PROTEIN 3ABC), SUBCELLULAR LOCATION (PROTEIN 3ABC), AND
INTERACTION WITH HUMAN MAVS (PROTEIN 3ABC).
STRAIN=HM175/18f;
PubMed=17438296; DOI=10.1073/pnas.0611506104;
Yang Y., Liang Y., Qu L., Chen Z., Yi M., Li K., Lemon S.M.;
"Disruption of innate immunity due to mitochondrial targeting of a
picornaviral protease precursor.";
Proc. Natl. Acad. Sci. U.S.A. 104:7253-7258(2007).
[34]
FUNCTION (PROTEASE 3C).
PubMed=17726047; DOI=10.1093/nar/gkm645;
Zhang B., Morace G., Gauss-Mueller V., Kusov Y.;
"Poly(A) binding protein, C-terminally truncated by the hepatitis A
virus proteinase 3C, inhibits viral translation.";
Nucleic Acids Res. 35:5975-5984(2007).
[35]
FUNCTION (PROTEIN 2B).
PubMed=18559929; DOI=10.1099/vir.0.83521-0;
Paulmann D., Magulski T., Schwarz R., Heitmann L., Flehmig B.,
Vallbracht A., Dotzauer A.;
"Hepatitis A virus protein 2B suppresses beta interferon (IFN) gene
transcription by interfering with IFN regulatory factor 3
activation.";
J. Gen. Virol. 89:1593-1604(2008).
[36]
PROTEOLYTIC CLEAVAGE (GENOME POLYPROTEIN), MUTAGENESIS OF ARG-769,
SUBUNIT (PROTEIN VP1-2A), AND PROTEOLYTIC CLEAVAGE (PROTEIN VP1-2A).
PubMed=18823593;
Morace G., Kusov Y., Dzagurov G., Beneduce F., Gauss-Muller V.;
"The unique role of domain 2A of the hepatitis A virus precursor
polypeptide P1-2A in viral morphogenesis.";
BMB Rep. 41:678-683(2008).
[37]
FUNCTION (PROTEIN 2B), AND SUBCELLULAR LOCATION (PROTEIN 2B).
PubMed=18216106; DOI=10.1128/JVI.02076-07;
de Jong A.S., de Mattia F., Van Dommelen M.M., Lanke K.,
Melchers W.J., Willems P.H., van Kuppeveld F.J.;
"Functional analysis of picornavirus 2B proteins: effects on calcium
homeostasis and intracellular protein trafficking.";
J. Virol. 82:3782-3790(2008).
[38]
FUNCTION (PROTEIN 3CD), AND MUTAGENESIS OF CYS-1691.
STRAIN=HM175/18f;
PubMed=21931545; DOI=10.1371/journal.ppat.1002169;
Qu L., Feng Z., Yamane D., Liang Y., Lanford R.E., Li K., Lemon S.M.;
"Disruption of TLR3 signaling due to cleavage of TRIF by the hepatitis
A virus protease-polymerase processing intermediate, 3CD.";
PLoS Pathog. 7:E1002169-E1002169(2011).
[39]
DOMAIN LATE-BUDDING (GENOME POLYPROTEIN), DOMAIN LATE-BUDDING (CAPSID
PROTEIN VP2), AND MUTAGENESIS OF TYR-167 AND TYR-200.
PubMed=23542590; DOI=10.1038/nature12029;
Feng Z., Hensley L., McKnight K.L., Hu F., Madden V., Ping L.,
Jeong S.H., Walker C., Lanford R.E., Lemon S.M.;
"A pathogenic picornavirus acquires an envelope by hijacking cellular
membranes.";
Nature 496:367-371(2013).
[40]
FUNCTION (PROTEASE 3C).
PubMed=24920812; DOI=10.1128/JVI.00869-14;
Wang D., Fang L., Wei D., Zhang H., Luo R., Chen H., Li K., Xiao S.;
"Hepatitis A virus 3C protease cleaves NEMO to impair induction of
beta interferon.";
J. Virol. 88:10252-10258(2014).
[41]
FUNCTION (VIRAL PROTEIN GENOME-LINKED).
PubMed=25240314; DOI=10.1016/j.coviro.2014.09.003;
Sun Y., Guo Y., Lou Z.;
"Formation and working mechanism of the picornavirus VPg uridylylation
complex.";
Curr. Opin. Virol. 9:24-30(2014).
[42]
FUNCTION (PROTEIN 2B), SUBUNIT (PROTEIN 2B), DOMAIN (PROTEIN 2B), AND
SUBCELLULAR LOCATION (PROTEIN 2B).
PubMed=26515753; DOI=10.1038/srep15884;
Shukla A., Dey D., Banerjee K., Nain A., Banerjee M.;
"The C-terminal region of the non-structural protein 2B from Hepatitis
A Virus demonstrates lipid-specific viroporin-like activity.";
Sci. Rep. 5:15884-15884(2015).
[43]
REVIEW.
PubMed=26999188; DOI=10.3390/v8030082;
Sun D., Chen S., Cheng A., Wang M.;
"Roles of the picornaviral 3C proteinase in the viral life cycle and
host cells.";
Viruses 8:82-82(2016).
[44]
PROTEOLYTIC CLEAVAGE (PROTEIN VP1-2A), SUBCELLULAR LOCATION (CAPSID
PROTEIN VP1), SUBCELLULAR LOCATION (CAPSID PROTEIN VP2), AND
SUBCELLULAR LOCATION (CAPSID PROTEIN VP3).
PubMed=28490497; DOI=10.1073/pnas.1619519114;
McKnight K.L., Xie L., Gonzalez-Lopez O., Rivera-Serrano E.E.,
Chen X., Lemon S.M.;
"Protein composition of the hepatitis A virus quasi-envelope.";
Proc. Natl. Acad. Sci. U.S.A. 114:6587-6592(2017).
[45]
FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), AND
FUNCTION (CAPSID PROTEIN VP3).
PubMed=29437974; DOI=10.1128/JVI.02065-17;
Costafreda M.I., Kaplan G.;
"HAVCR1 (CD365) and its mouse ortholog are functional hepatitis A
virus (HAV) cellular receptors that mediate HAV infection.";
J. Virol. 92:0-0(2018).
[46]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1520-1736.
PubMed=8164744; DOI=10.1038/369072a0;
Allaire M., Chernaia M.M., Malcolm B.A., James M.N.;
"Picornaviral 3C cysteine proteinases have a fold similar to
chymotrypsin-like serine proteinases.";
Nature 369:72-76(1994).
[47]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1520-1736, RNA-BINDING
(PROTEASE 3C), AND FUNCTION (PROTEASE 3C).
PubMed=9032381;
Bergmann E.M., Mosimann S.C., Chernaia M.M., Malcolm B.A.,
James M.N.G.;
"The refined crystal structure of the 3C gene product from hepatitis A
virus: specific proteinase activity and RNA recognition.";
J. Virol. 71:2436-2448(1997).
[48]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1520-1736 IN COMPLEX WITH THE
INHIBITOR IODOACETYL-VALYL-PHENYLALANYL-AMIDE.
PubMed=10603326; DOI=10.1006/viro.1999.9968;
Bergmann E.M., Cherney M.M., Mckendrick J., Frormann S., Luo C.,
Malcolm B.A., Vederas J.C., James M.N.G.;
"Crystal structure of an inhibitor complex of the 3C proteinase from
hepatitis A virus (HAV) and implications for the polyprotein
processing in HAV.";
Virology 265:153-163(1999).
[49]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) OF 1520-1731 IN COMPLEX WITH
PEPTIDE-BASED KETONE INHIBITORS.
PubMed=16860823; DOI=10.1016/j.jmb.2006.06.047;
Yin J., Cherney M.M., Bergmann E.M., Zhang J., Huitema C.,
Pettersson H., Eltis L.D., Vederas J.C., James M.N.G.;
"An episulfide cation (thiiranium ring) trapped in the active site of
HAV 3C proteinase inactivated by peptide-based ketone inhibitors.";
J. Mol. Biol. 361:673-686(2006).
[50] {ECO:0000244|PDB:4WZN}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 765-981, AND SUBUNIT
(PROTEIN 2B).
PubMed=25589659; DOI=10.1128/JVI.02881-14;
Vives-Adrian L., Garriga D., Buxaderas M., Fraga J., Pereira P.J.,
Macedo-Ribeiro S., Verdaguer N.;
"Structural basis for host membrane remodeling induced by protein 2B
of hepatitis A virus.";
J. Virol. 89:3648-3658(2015).
[51]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 24-245 AND 246-491, FUNCTION
(PROTEIN VP0), SUBCELLULAR LOCATION (PROTEIN VP4), INTERACTION WITH
CAPSID PROTEIN VP2 (CAPSID PROTEIN VP1), INTERACTION WITH CAPSID
PROTEIN VP2 (CAPSID PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP1
(CAPSID PROTEIN VP2), INTERACTION WITH CAPSID PROTEIN VP1(CAPSID
PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP3 (CAPSID PROTEIN
VP1), INTERACTION WITH CAPSID PROTEIN VP3 (CAPSID PROTEIN VP2),
FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN VP2), FUNCTION
(CAPSID PROTEIN VP3), SUBCELLULAR LOCATION (CAPSID PROTEIN VP1),
SUBCELLULAR LOCATION (CAPSID PROTEIN VP2), AND SUBCELLULAR LOCATION
(CAPSID PROTEIN VP3).
STRAIN=TZ84;
PubMed=25327248; DOI=10.1038/nature13806;
Wang X., Ren J., Gao Q., Hu Z., Sun Y., Li X., Rowlands D.J., Yin W.,
Wang J., Stuart D.I., Rao Z., Fry E.E.;
"Hepatitis A virus and the origins of picornaviruses.";
Nature 517:85-88(2015).
[52] {ECO:0000244|PDB:5WTE, ECO:0000244|PDB:5WTF, ECO:0000244|PDB:5WTH}
STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 492-769; 24-245
AND 246-491, INTERACTION WITH CAPSID PROTEIN VP2 (CAPSID PROTEIN VP1),
INTERACTION WITH CAPSID PROTEIN VP2 (CAPSID PROTEIN VP3), INTERACTION
WITH CAPSID PROTEIN VP1 (CAPSID PROTEIN VP2), INTERACTION WITH CAPSID
PROTEIN VP1(CAPSID PROTEIN VP3), INTERACTION WITH CAPSID PROTEIN VP3
(CAPSID PROTEIN VP1), INTERACTION WITH CAPSID PROTEIN VP3 (CAPSID
PROTEIN VP2), FUNCTION (CAPSID PROTEIN VP1), FUNCTION (CAPSID PROTEIN
VP2), FUNCTION (CAPSID PROTEIN VP3), SUBCELLULAR LOCATION (CAPSID
PROTEIN VP1), SUBCELLULAR LOCATION (CAPSID PROTEIN VP2), AND
SUBCELLULAR LOCATION (CAPSID PROTEIN VP3).
PubMed=28074040; DOI=10.1073/pnas.1616502114;
Wang X., Zhu L., Dang M., Hu Z., Gao Q., Yuan S., Sun Y., Zhang B.,
Ren J., Kotecha A., Walter T.S., Wang J., Fry E.E., Stuart D.I.,
Rao Z.;
"Potent neutralization of hepatitis A virus reveals a receptor mimic
mechanism and the receptor recognition site.";
Proc. Natl. Acad. Sci. U.S.A. 114:770-775(2017).
-!- FUNCTION: Capsid protein VP1: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome (PubMed:25327248, PubMed:28074040). All these proteins
contain a beta-sheet structure called beta-barrel jelly roll
(PubMed:25327248). Together they form an icosahedral capsid (T=3)
composed of 60 copies of each VP1, VP2, and VP3, with a diameter
of approximately 300 Angstroms (PubMed:25327248). VP1 is situated
at the 12 fivefold axes, whereas VP2 and VP3 are located at the
quasi-sixfold axes (PubMed:25327248). The naked capsid interacts
with the host receptor HAVCR1 to provide virion attachment to and
probably entry into the target cell (PubMed:9658108,
PubMed:11134285, PubMed:29437974). {ECO:0000269|PubMed:11134285,
ECO:0000269|PubMed:25327248, ECO:0000269|PubMed:28074040,
ECO:0000269|PubMed:29437974, ECO:0000269|PubMed:9658108}.
-!- FUNCTION: Capsid protein VP2: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome (PubMed:25327248, PubMed:28074040). All these proteins
contain a beta-sheet structure called beta-barrel jelly roll
(PubMed:25327248). Together they form an icosahedral capsid (T=3)
composed of 60 copies of each VP1, VP2, and VP3, with a diameter
of approximately 300 Angstroms (PubMed:25327248). VP1 is situated
at the 12 fivefold axes, whereas VP2 and VP3 are located at the
quasi-sixfold axes (PubMed:25327248). The naked capsid interacts
with the host receptor HAVCR1 to provide virion attachment to and
probably entry into the target cell (PubMed:9658108,
PubMed:11134285, PubMed:29437974). {ECO:0000269|PubMed:11134285,
ECO:0000269|PubMed:25327248, ECO:0000269|PubMed:28074040,
ECO:0000269|PubMed:29437974, ECO:0000269|PubMed:9658108}.
-!- FUNCTION: Capsid protein VP3: Capsid proteins VP1, VP2, and VP3
form a closed capsid enclosing the viral positive strand RNA
genome (PubMed:25327248, PubMed:28074040). All these proteins
contain a beta-sheet structure called beta-barrel jelly roll
(PubMed:25327248). Together they form an icosahedral capsid (T=3)
composed of 60 copies of each VP1, VP2, and VP3, with a diameter
of approximately 300 Angstroms (PubMed:25327248). VP1 is situated
at the 12 fivefold axes, whereas VP2 and VP3 are located at the
quasi-sixfold axes (PubMed:25327248). The naked capsid interacts
with the host receptor HAVCR1 to provide virion attachment to and
probably entry into the target cell (PubMed:9658108,
PubMed:11134285, PubMed:29437974). {ECO:0000269|PubMed:11134285,
ECO:0000269|PubMed:25327248, ECO:0000269|PubMed:28074040,
ECO:0000269|PubMed:29437974, ECO:0000269|PubMed:9658108}.
-!- FUNCTION: Protein VP0: VP0 precursor is a component of the
immature procapsids. {ECO:0000269|PubMed:25327248}.
-!- FUNCTION: Protein VP4: Plays a role in the assembly of the 12
pentamers into an icosahedral structure. Has not been detected in
mature virions, supposedly owing to its small size.
{ECO:0000269|PubMed:9988685}.
-!- FUNCTION: Protein VP1-2A: Precursor component of immature
procapsids that corresponds to an extended form of the structural
protein VP1 (PubMed:9988685, PubMed:12097562). After maturation,
possibly by the host Cathepsin L, the assembly signal 2A is
cleaved to give rise to the mature VP1 protein (PubMed:9988685).
{ECO:0000269|PubMed:12097562, ECO:0000269|PubMed:9988685}.
-!- FUNCTION: Protein 2B: Function as a viroporin (PubMed:26515753).
Affects membrane integrity and causes an increase in membrane
permeability (PubMed:9875331). Involved in host intracellular
membrane rearrangements probably to give rise to the viral
factories (PubMed:9344908). Does not disrupt calcium homeostasis
or glycoprotein trafficking (PubMed:18216106). Antagonizes the
innate immune response of the host by suppressing IFN-beta
synthesis, which it achieves by interfering with the DDX58/IFIH1
(RIG-I/MDA5) pathway (PubMed:18559929).
{ECO:0000269|PubMed:18216106, ECO:0000269|PubMed:18559929,
ECO:0000269|PubMed:26515753, ECO:0000269|PubMed:9344908,
ECO:0000269|PubMed:9875331}.
-!- FUNCTION: Protein 2BC: Affects membrane integrity and causes an
increase in membrane permeability. {ECO:0000269|PubMed:9344908,
ECO:0000269|PubMed:9875331}.
-!- FUNCTION: Protein 2C: Associates with and induces structural
rearrangements of intracellular membranes (PubMed:9344908).
Displays RNA-binding activity (PubMed:9645199).
{ECO:0000269|PubMed:9344908, ECO:0000269|PubMed:9645199}.
-!- FUNCTION: Protein 3ABC: The precursor 3ABC is targeted to the
mitochondrial membrane where protease 3C activity cleaves and
inhibits the host antiviral protein MAVS, thereby disrupting
activation of IRF3 through the IFIH1/MDA5 pathway
(PubMed:17438296). In vivo, the protease activity of 3ABC
precursor is more efficient in cleaving the 2BC precursor than
that of protein 3C. The 3ABC precursor may therefore play a role
in the proteolytic processing of the polyprotein
(PubMed:10559299). {ECO:0000269|PubMed:10559299,
ECO:0000269|PubMed:17438296}.
-!- FUNCTION: Protein 3AB: Interacts with the 3CD precursor and with
RNA structures found at both the 5'- and 3'-termini of the viral
genome (PubMed:10562502). Since the 3AB precursor contains the
hydrophobic domain 3A, it probably anchors the whole viral
replicase complex to intracellular membranes on which viral RNA
synthesis occurs (PubMed:9705870). {ECO:0000269|PubMed:10562502,
ECO:0000269|PubMed:9705870}.
-!- FUNCTION: Protein 3A: May serve as membrane anchor to the 3AB and
3ABC precursors via its hydrophobic domain (PubMed:9705870). May
interact with RNA (PubMed:10562502). {ECO:0000269|PubMed:10562502,
ECO:0000269|PubMed:9705870}.
-!- FUNCTION: Viral protein genome-linked: Acts as a primer for viral
RNA replication and remains covalently bound to viral genomic RNA.
VPg is uridylylated prior to priming replication into VPg-pUpU.
The VPg-pUpU is then used as primer on the genomic RNA poly(A) by
the RNA-dependent RNA polymerase to replicate the viral genome.
{ECO:0000250|UniProtKB:P03300, ECO:0000303|PubMed:25240314}.
-!- FUNCTION: Protease 3C: Cysteine protease that generates mature
viral proteins from the precursor polyprotein (PubMed:1850033). In
addition to its proteolytic activity, it binds to viral RNA, and
thus influences viral genome replication (PubMed:15361063). RNA
and substrate bind cooperatively to the protease (PubMed:9032381).
Cleaves IKBKG/NEMO to impair innate immune signaling
(PubMed:24920812). Cleaves host PABPC1 which may participate to
the switch of viral translation to RNA synthesis
(PubMed:17726047). {ECO:0000269|PubMed:15361063,
ECO:0000269|PubMed:17726047, ECO:0000269|PubMed:1850033,
ECO:0000269|PubMed:24920812, ECO:0000269|PubMed:9032381}.
-!- FUNCTION: Protein 3CD: Interacts with the 3AB precursor and with
RNA structures found at both the 5'- and 3'-termini of the viral
genome (PubMed:10562502). Disrupts TLR3 signaling by degrading the
host adapter protein TICAM1/TRIF (PubMed:21931545).
{ECO:0000269|PubMed:10562502, ECO:0000269|PubMed:21931545}.
-!- FUNCTION: RNA-directed RNA polymerase 3D-POL replicates genomic
and antigenomic RNA by recognizing replications specific signals.
{ECO:0000305}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539,
ECO:0000269|PubMed:8291234}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Gln-|-Gly bond in the
poliovirus polyprotein. In other picornavirus reactions Glu may be
substituted for Gln, and Ser or Thr for Gly.
{ECO:0000269|PubMed:1850033}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- SUBUNIT: Protein 2B: Homodimer. Homomultimer; probably interacts
with membranes in a multimeric form (PubMed:26515753). Seems to
assemble into amyloid-like fibers (PubMed:25589659). Protein 3AB:
Homodimer. Monomer (PubMed:9705870). Protein 3AB: Interacts with
protein 3CD (PubMed:10562502). Protein 3CD: Interacts with protein
3AB (PubMed:10562502). Protein 3ABC: Interacts with human MAVS
(PubMed:17438296). Protease 3C: Homodimer; disulfide-linked
(PubMed:15361063). Protein VP1-2A: Homopentamer (PubMed:12782637).
Protein VP1-2A: Homooligomer (PubMed:18823593, PubMed:12782637).
Capsid protein VP1: Interacts with capsid protein VP2
(PubMed:25327248, PubMed:28074040). Capsid protein VP1: Interacts
with capsid protein VP3 (PubMed:25327248, PubMed:28074040). Capsid
protein VP2: Interacts with capsid protein VP1 (PubMed:25327248,
PubMed:28074040). Capsid protein VP2: Interacts with capsid
protein VP3 (PubMed:25327248, PubMed:28074040). Capsid protein
VP3: Interacts with capsid protein VP1 (PubMed:25327248,
PubMed:28074040). Capsid protein VP3: Interacts with capsid
protein VP2 (PubMed:25327248, PubMed:28074040).
{ECO:0000269|PubMed:10562502, ECO:0000269|PubMed:12782637,
ECO:0000269|PubMed:15361063, ECO:0000269|PubMed:17438296,
ECO:0000269|PubMed:18823593, ECO:0000269|PubMed:25327248,
ECO:0000269|PubMed:25589659, ECO:0000269|PubMed:26515753,
ECO:0000269|PubMed:28074040, ECO:0000269|PubMed:9705870}.
-!- SUBCELLULAR LOCATION: Capsid protein VP2: Virion
{ECO:0000269|PubMed:25327248, ECO:0000269|PubMed:28074040}. Host
endosome, host multivesicular body {ECO:0000269|PubMed:28490497}.
Note=The egress of newly formed virions occurs through an exosome-
like mechanism involving endosomal budding of viral capsids into
multivesicular bodies. {ECO:0000269|PubMed:28490497}.
-!- SUBCELLULAR LOCATION: Capsid protein VP3: Virion
{ECO:0000269|PubMed:25327248, ECO:0000269|PubMed:28074040}. Host
endosome, host multivesicular body {ECO:0000269|PubMed:28490497}.
Note=The egress of newly formed virions occurs through an exosome-
like mechanism involving endosomal budding of viral capsids into
multivesicular bodies. {ECO:0000269|PubMed:28490497}.
-!- SUBCELLULAR LOCATION: Capsid protein VP1: Virion
{ECO:0000269|PubMed:25327248, ECO:0000269|PubMed:28074040}. Host
endosome, host multivesicular body {ECO:0000269|PubMed:28490497}.
Note=The egress of newly formed virions occurs through an exosome-
like mechanism involving endosomal budding of viral capsids into
multivesicular bodies. {ECO:0000269|PubMed:28490497}.
-!- SUBCELLULAR LOCATION: Protein VP4: Virion
{ECO:0000269|PubMed:25327248}. Note=Present in the full mature
virion (PubMed:25327248). The egress of newly formed virions
occurs through an exosome-like mechanism involving endosomal
budding of viral capsids into multivesicular bodies (Probable).
{ECO:0000269|PubMed:25327248, ECO:0000305|PubMed:28490497}.
-!- SUBCELLULAR LOCATION: Protein 2B: Host membrane
{ECO:0000269|PubMed:18216106, ECO:0000269|PubMed:26515753,
ECO:0000269|PubMed:9875331}; Peripheral membrane protein
{ECO:0000269|PubMed:9875331}. Note=Probably localizes to
intracellular membrane vesicles that are induced after virus
infection as the site for viral RNA replication. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 2C: Host membrane
{ECO:0000269|PubMed:9645199}; Single-pass membrane protein
{ECO:0000269|PubMed:9875331}. Note=Probably localizes to
intracellular membrane vesicles that are induced after virus
infection as the site for viral RNA replication. May associate
with membranes through a N-terminal amphipathic helix.
{ECO:0000305|PubMed:9645199}.
-!- SUBCELLULAR LOCATION: Protein 3ABC: Host membrane {ECO:0000305};
Single-pass membrane protein {ECO:0000255}. Host mitochondrion
outer membrane {ECO:0000269|PubMed:17438296}; Single-pass membrane
protein {ECO:0000305}. Note=Probably localizes to intracellular
membrane vesicles that are induced after virus infection as the
site for viral RNA replication. {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3AB: Host membrane {ECO:0000305};
Single-pass membrane protein {ECO:0000255}. Note=Probably
localizes to intracellular membrane vesicles that are induced
after virus infection as the site for viral RNA replication.
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protein 3A: Host membrane {ECO:0000305};
Single-pass membrane protein {ECO:0000255}. Note=Probably
localizes to intracellular membrane vesicles that are induced
after virus infection as the site for viral RNA replication.
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Viral protein genome-linked: Virion
{ECO:0000305}.
-!- SUBCELLULAR LOCATION: Protease 3C: Host cytoplasm {ECO:0000305}.
-!- SUBCELLULAR LOCATION: RNA-directed RNA polymerase 3D-POL: Host
cytoplasmic vesicle membrane {ECO:0000305}; Peripheral membrane
protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Note=Interacts with membranes in a complex with viral protein 3AB.
Probably localizes to the surface of intracellular membrane
vesicles that are induced after virus infection as the site for
viral RNA replication. These vesicles are derived from the
endoplasmic reticulum. {ECO:0000305}.
-!- DOMAIN: Protein VP1-2A: The assembly signal 2A region mediates
pentamerization of P1-2A. {ECO:0000269|PubMed:12097562,
ECO:0000269|PubMed:12782637}.
-!- DOMAIN: Genome polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding
(Probable). They recruit proteins of the host ESCRT machinery
(Endosomal Sorting Complex Required for Transport) or ESCRT-
associated proteins (Probable). The genome polyprotein contains
two L domains: a tandem of (L)YPX(n)L domain which is known to
bind the PDCD6IP/ALIX adaptater protein (PubMed:23542590).
{ECO:0000269|PubMed:23542590, ECO:0000305}.
-!- DOMAIN: Capsid protein VP2: Late-budding domains (L domains) are
short sequence motifs essential for viral particle budding
(Probable). They recruit proteins of the host ESCRT machinery
(Endosomal Sorting Complex Required for Transport) or ESCRT-
associated proteins (Probable). Capsid protein VP2 contains two L
domains: a tandem of (L)YPX(n)L domain which is known to bind the
Alix adaptater protein (PubMed:23542590).
{ECO:0000269|PubMed:23542590, ECO:0000305}.
-!- DOMAIN: Protein 2B: The C-terminus displays a membrane-penetrating
ability. {ECO:0000269|PubMed:26515753}.
-!- PTM: Genome polyprotein: Specific enzymatic cleavages by viral
protease in vivo yield a variety of precursors and mature
proteins. Polyprotein processing intermediates are produced, such
as P1-2A which is a functional precursor of the structural
proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC
precursor which is a stable and catalytically active precursor of
3A, 3B and 3C proteins, 3AB and 3CD precursors (PubMed:7483265,
PubMed:1850033, PubMed:8382411, PubMed:8291234, PubMed:9060697,
PubMed:9733840, PubMed:8259663, PubMed:7853510, PubMed:10559299).
The assembly signal 2A is removed from VP1-2A by a host protease,
possibly host Cathepsin L (PubMed:18823593). This cleavage occurs
over a region of 3 amino-acids probably generating VP1 proteins
with heterogeneous C-termini (PubMed:10364353). During virion
maturation, non-infectious particles are rendered infectious
following cleavage of VP0. This maturation cleavage is followed by
a conformational change of the particle (PubMed:12782637,
PubMed:8291234, PubMed:9060697, PubMed:9733840).
{ECO:0000269|PubMed:10364353, ECO:0000269|PubMed:10559299,
ECO:0000269|PubMed:12782637, ECO:0000269|PubMed:1850033,
ECO:0000269|PubMed:18823593, ECO:0000269|PubMed:7483265,
ECO:0000269|PubMed:7853510, ECO:0000269|PubMed:8259663,
ECO:0000269|PubMed:8291234, ECO:0000269|PubMed:8382411,
ECO:0000269|PubMed:9060697, ECO:0000269|PubMed:9733840}.
-!- PTM: Protein VP1-2A: The assembly signal 2A is removed from VP1-2A
by a host protease, possibly host Cathepsin L in nacked virions
(PubMed:18823593). This cleavage does not occur in enveloped
virions (PubMed:28490497). This cleavage occurs over a region of 3
amino-acids probably generating VP1 proteins with heterogeneous C-
termini (PubMed:10364353). {ECO:0000269|PubMed:10364353,
ECO:0000269|PubMed:18823593, ECO:0000269|PubMed:28490497}.
-!- PTM: Viral protein genome-linked: VPg is uridylylated prior to
priming replication into VPg-pUpU. {ECO:0000250|UniProtKB:P03300}.
-!- PTM: Protein VP4: Unlike other picornaviruses, does not seem to be
myristoylated. {ECO:0000269|PubMed:8389076}.
-!- MISCELLANEOUS: The need for an intact eIF4G factor for the
initiation of translation of HAV results in an inability to shut
off host protein synthesis by a mechanism similar to that of other
picornaviruses. {ECO:0000305}.
-!- MISCELLANEOUS: During infection, enveloped virions (eHAV) are
released from cells (PubMed:23542590). These eHAV are cloaked in
host-derived membranes and resemble exosomes (PubMed:28490497).
The membrane of eHAV is devoid of viral proteins and thus prevents
their neutralization by antibodies (PubMed:23542590). eHAV budding
is dependent on ESCRT-associated proteins VPS4B and PDCD6IP/ALIX
(PubMed:23542590). eHAV are produced and released in the serum and
plasma, but not in bile and feces which only contain the naked,
nonenveloped virions (Probable). It is likely that eHAV also use
HAVCR1 as a functional receptor to infect cells, an evolutionary
trait that may enhance HAV infectivity (PubMed:29437974).
{ECO:0000269|PubMed:23542590, ECO:0000269|PubMed:28490497,
ECO:0000269|PubMed:29437974, ECO:0000303|PubMed:23542590,
ECO:0000305}.
-!- MISCELLANEOUS: Wild-type HM175 (HM175/wt) comes from a sample
isolated from a patient in Australia in 1976 and subsequently
passaged three times in marmosets. HM175/7 is an attenuated strain
derived from HM175 by 32 passages in African green monkey kidney
cells. HM175/18f, HM175/24a, and HM175/43c are cytopathic isolates
derived from HM175 by serial passages in FRhK-4 cells.
{ECO:0000305}.
-!- MISCELLANEOUS: Mutations in proteins 2B and 2C seem to be
essential for strain HM175 adaptation to growth in cell culture.
-!- SIMILARITY: Belongs to the picornaviridae polyprotein family.
{ECO:0000305}.
-!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
In vitro, both are used, with a preference for Met-3.
{ECO:0000269|PubMed:1310188}.
-!- SEQUENCE CAUTION:
Sequence=AAA45466.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M14707; AAA45465.1; -; Genomic_RNA.
EMBL; M14707; AAA45466.1; ALT_INIT; Genomic_RNA.
EMBL; M16632; AAA45471.1; -; Genomic_RNA.
EMBL; M59808; AAA45467.1; -; Genomic_RNA.
EMBL; M59809; AAA45469.1; -; Genomic_RNA.
EMBL; M59810; AAA45468.1; -; Genomic_RNA.
EMBL; M14114; AAA45475.1; -; Genomic_RNA.
EMBL; M14115; AAA45476.1; -; Genomic_RNA.
EMBL; K00386; -; NOT_ANNOTATED_CDS; Genomic_RNA.
EMBL; AF396398; AAL66215.1; -; Genomic_RNA.
PIR; A03905; A03905.
PIR; A25981; GNNYHM.
PIR; A94149; GNNYMK.
PIR; JH0135; JH0135.
PIR; PQ0427; PQ0427.
PIR; PQ0428; PQ0428.
PIR; PQ0431; PQ0431.
RefSeq; NP_041007.1; NC_001489.1.
RefSeq; NP_041008.1; NC_001489.1.
PDB; 1HAV; X-ray; 2.00 A; A/B=1520-1736.
PDB; 1QA7; X-ray; 1.90 A; A/B/C/D=1520-1736.
PDB; 2H6M; X-ray; 1.40 A; A=1520-1731.
PDB; 2H9H; X-ray; 1.39 A; A=1520-1731.
PDB; 2HAL; X-ray; 1.35 A; A=1520-1731.
PDB; 4QPG; X-ray; 3.50 A; B=41-244, C=246-491.
PDB; 4QPI; X-ray; 3.01 A; B=24-245, C=246-491.
PDB; 4WZN; X-ray; 2.70 A; A/B=765-981.
PDB; 5WTE; EM; 3.40 A; A=492-769, B=24-245, C=246-491.
PDB; 5WTF; EM; 3.90 A; A=540-763, B=42-244, C=246-491.
PDB; 5WTH; EM; 4.20 A; A=492-769, B=24-245, C=246-491.
PDBsum; 1HAV; -.
PDBsum; 1QA7; -.
PDBsum; 2H6M; -.
PDBsum; 2H9H; -.
PDBsum; 2HAL; -.
PDBsum; 4QPG; -.
PDBsum; 4QPI; -.
PDBsum; 4WZN; -.
PDBsum; 5WTE; -.
PDBsum; 5WTF; -.
PDBsum; 5WTH; -.
ProteinModelPortal; P08617; -.
SMR; P08617; -.
DrugBank; DB04634; N-BENZYLOXYCARBONYL-L-SERINE-BETALACTONE.
DrugBank; DB04029; Phenylalanine Amide.
PRIDE; P08617; -.
GeneID; 1493918; -.
GeneID; 1493919; -.
KEGG; vg:1493918; -.
KEGG; vg:1493919; -.
OrthoDB; VOG090000BA; -.
EvolutionaryTrace; P08617; -.
Proteomes; UP000006724; Genome.
Proteomes; UP000096966; Genome.
Proteomes; UP000139151; Genome.
Proteomes; UP000155985; Genome.
Proteomes; UP000157977; Genome.
GO; GO:0044162; C:host cell cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0044193; C:host cell mitochondrial outer membrane; IEA:UniProtKB-SubCell.
GO; GO:0044385; C:integral to membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0005216; F:ion channel activity; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0039707; P:pore formation by virus in membrane of host cell; IEA:UniProtKB-KW.
GO; GO:0051259; P:protein complex oligomerization; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0039657; P:suppression by virus of host gene expression; IEA:UniProtKB-KW.
GO; GO:0039545; P:suppression by virus of host MAVS activity; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
CDD; cd00205; rhv_like; 2.
Gene3D; 2.60.120.20; -; 3.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR024354; Hepatitis_A_VP1-2A.
InterPro; IPR000199; Peptidase_C3A/C3B_picornavir.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001676; Picornavirus_capsid.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
InterPro; IPR029053; Viral_coat.
Pfam; PF12944; HAV_VP; 1.
Pfam; PF00548; Peptidase_C3; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00073; Rhv; 2.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Capsid protein; Complete proteome;
Covalent protein-RNA linkage; Direct protein sequencing;
Disulfide bond; Helicase; Host cytoplasm; Host cytoplasmic vesicle;
Host endosome; Host membrane; Host mitochondrion;
Host mitochondrion outer membrane; Host-virus interaction; Hydrolase;
Inhibition of host innate immune response by virus;
Inhibition of host MAVS by virus;
Inhibition of host RLR pathway by virus;
Interferon antiviral system evasion; Ion channel; Ion transport;
Membrane; Nucleotide-binding; Nucleotidyltransferase; Phosphoprotein;
Protease; Reference proteome; RNA-binding;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Transmembrane; Transmembrane helix; Transport;
Viral attachment to host cell; Viral immunoevasion; Viral ion channel;
Viral RNA replication; Virion; Virus entry into host cell.
CHAIN 1 2227 Genome polyprotein.
/FTId=PRO_0000308969.
CHAIN 1 245 Protein VP0.
/FTId=PRO_0000308970.
CHAIN 1 23 Protein VP4.
/FTId=PRO_0000039946.
CHAIN 24 245 Capsid protein VP2.
/FTId=PRO_0000039947.
CHAIN 246 491 Capsid protein VP3.
/FTId=PRO_0000039948.
CHAIN 492 836 Protein VP1-2A.
/FTId=PRO_0000308971.
CHAIN 492 765 Capsid protein VP1.
/FTId=PRO_0000039949.
CHAIN 766 836 Assembly signal 2A.
/FTId=PRO_0000039950.
CHAIN 837 1422 Protein 2BC.
/FTId=PRO_0000308972.
CHAIN 837 1087 Protein 2B.
/FTId=PRO_0000039951.
CHAIN 1088 1422 Protein 2C.
/FTId=PRO_0000039952.
CHAIN 1423 2227 Protein 3ABCD.
/FTId=PRO_0000308973.
CHAIN 1423 1738 Protein 3ABC.
/FTId=PRO_0000308974.
CHAIN 1423 1519 Protein 3AB.
/FTId=PRO_0000308975.
CHAIN 1423 1496 Protein 3A.
/FTId=PRO_0000039953.
CHAIN 1497 1519 Viral protein genome-linked.
/FTId=PRO_0000039954.
CHAIN 1520 2227 Protein 3CD.
/FTId=PRO_0000308976.
CHAIN 1520 1738 Protease 3C.
/FTId=PRO_0000039955.
CHAIN 1739 2227 RNA-directed RNA polymerase 3D-POL.
/FTId=PRO_0000039956.
TRANSMEM 1011 1031 Helical. {ECO:0000255}.
TRANSMEM 1462 1482 Helical. {ECO:0000255,
ECO:0000269|PubMed:9705870}.
DOMAIN 1204 1366 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1520 1716 Peptidase C3. {ECO:0000255}.
DOMAIN 1976 2097 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 1230 1237 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
REGION 766 836 Involved in P1-2A pentamerization.
{ECO:0000269|PubMed:12097562,
ECO:0000269|PubMed:12782637}.
REGION 1043 1070 Membrane-penetrating ability.
{ECO:0000269|PubMed:26515753}.
MOTIF 167 171 (L)YPX(n)L motif.
{ECO:0000269|PubMed:23542590}.
MOTIF 200 205 (L)YPX(n)L motif.
{ECO:0000269|PubMed:23542590}.
ACT_SITE 1563 1563 For protease 3C activity.
{ECO:0000250|UniProtKB:P13901}.
ACT_SITE 1603 1603 For protease 3C activity.
{ECO:0000250|UniProtKB:P13901}.
ACT_SITE 1691 1691 For protease 3C activity.
{ECO:0000250|UniProtKB:P13901}.
SITE 245 246 Cleavage; by protease 3C.
{ECO:0000303|PubMed:10559299}.
SITE 491 492 Cleavage; by protease 3C.
{ECO:0000303|PubMed:10559299}.
SITE 765 766 Cleavage; partial; by host.
{ECO:0000269|PubMed:10364353,
ECO:0000269|PubMed:12782637}.
SITE 769 769 Important for VP1 folding and capsid
assembly. {ECO:0000269|PubMed:12782637,
ECO:0000269|PubMed:18823593}.
SITE 836 837 Cleavage; by protease 3C.
{ECO:0000269|PubMed:7483265,
ECO:0000269|PubMed:7853510}.
SITE 1087 1088 Cleavage; by protease 3C.
{ECO:0000269|PubMed:7853510}.
SITE 1422 1423 Cleavage; by protease 3C.
{ECO:0000303|PubMed:10559299}.
SITE 1496 1497 Cleavage; by protease 3C.
{ECO:0000269|PubMed:10559299}.
SITE 1519 1520 Cleavage; by protease 3C.
{ECO:0000269|PubMed:10559299}.
SITE 1738 1739 Cleavage; by protease 3C.
{ECO:0000269|PubMed:8291234}.
MOD_RES 1499 1499 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
DISULFID 1543 1543 Interchain.
{ECO:0000269|PubMed:15361063}.
VARIANT 77 77 K -> R (in strain: HM175/7, HM175/18f,
HM175/24a and HM175/43c).
VARIANT 315 315 D -> A (in strain: HM175/24a and HM175/
43c).
VARIANT 336 336 T -> K (in strain: HM175/18f).
VARIANT 638 638 I -> V (in strain: HM175/24a).
VARIANT 688 688 N -> S (in strain: HM175/24a and HM175/
43c).
VARIANT 762 762 S -> P (in strain: HM175/18f).
VARIANT 764 764 E -> V (in strain: HM175/7).
VARIANT 767 767 M -> V (in strain: HM175/24a and HM175/
43c).
VARIANT 821 821 N -> S (in strain: HM175/7).
VARIANT 838 838 K -> N (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 849 849 I -> M (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 941 941 D -> E (in 24).
VARIANT 993 993 D -> H (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1052 1052 A -> V (in strain: HM175/7, HM175/18f,
HM175/24a and HM175/43c).
VARIANT 1062 1062 G -> A (in strain: HM175/7).
VARIANT 1109 1111 AIY -> GIC (in strain: HM175/18f, HM175/
24a and HM175/43c).
VARIANT 1118 1118 K -> M (in strain: HM175/7).
VARIANT 1151 1151 E -> K (in strain: HM175/7, HM175/18f,
HM175/24a and HM175/43c).
VARIANT 1163 1163 F -> S (in strain: HM175/7, HM175/18f,
HM175/24a and HM175/43c).
VARIANT 1180 1180 H -> Y (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1212 1212 S -> F (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1229 1229 Y -> H (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1277 1277 V -> I (in strain: HM175/7).
VARIANT 1407 1407 E -> D (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1428 1428 Missing (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1480 1480 F -> V (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1487 1487 R -> H (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1500 1500 H -> Y (in strain: HM175/7).
VARIANT 1507 1507 Q -> H (in strain: HM175/18f, HM175/24a
and HM175/43c).
VARIANT 1524 1524 I -> V (in strain: HM175/43c).
VARIANT 1620 1620 Q -> E (in strain: HM175/18f and HM175/
24a).
VARIANT 1675 1675 T -> A (in strain: HM175/43c).
VARIANT 1805 1805 D -> G (in strain: HM175/7, HM175/18f,
HM175/24a and HM175/43c).
VARIANT 1930 1930 S -> T (in strain: HM175/7, HM175/18f,
HM175/24a and HM175/43c).
VARIANT 1962 1962 R -> K (in strain: HM175/18f, HM175/24a
and HM175/43c).
MUTAGEN 167 167 Y->A: Severely decreases virus release
but does not impair viral RNA
replication.
{ECO:0000269|PubMed:23542590}.
MUTAGEN 200 200 Y->A: Severely decreases virus release
but does not impair viral RNA
replication.
{ECO:0000269|PubMed:23542590}.
MUTAGEN 769 769 R->M: Complete loss of viral particles
assembly. Interferes with oligomerization
of protein VP1-2A and maturation of
procapsids. {ECO:0000269|PubMed:12782637,
ECO:0000269|PubMed:18823593}.
MUTAGEN 836 836 Q->N: Partial loss of VP1-2A-2B cleavage.
{ECO:0000269|PubMed:7483265}.
MUTAGEN 836 836 Q->R: Complete loss of VP1-2A-2B
cleavage. {ECO:0000269|PubMed:7483265}.
MUTAGEN 1052 1052 A->I,L,V: 10-20 fold increase in virus
yield. {ECO:0000269|PubMed:12858403}.
MUTAGEN 1543 1543 C->S: Complete loss of protease 3C
dimerization.
{ECO:0000269|PubMed:15361063}.
MUTAGEN 1691 1691 C->A: Complete loss of enzymatic
activity. Complete loss of cleavage of
host TICAM1.
{ECO:0000269|PubMed:21931545}.
MUTAGEN 1691 1691 C->A: Complete loss of proteolytic
activity. {ECO:0000269|PubMed:15361063}.
CONFLICT 67 67 R -> K (in Ref. 7; AAL66215).
{ECO:0000305}.
CONFLICT 1825 1825 D -> V (in Ref. 4; AAA45476).
{ECO:0000305}.
CONFLICT 1850 1850 G -> R (in Ref. 4; AAA45476).
{ECO:0000305}.
CONFLICT 1856 1856 E -> G (in Ref. 4; AAA45476).
{ECO:0000305}.
STRAND 38 40 {ECO:0000244|PDB:5WTE}.
STRAND 47 51 {ECO:0000244|PDB:5WTE}.
HELIX 76 79 {ECO:0000244|PDB:5WTE}.
STRAND 84 92 {ECO:0000244|PDB:5WTE}.
STRAND 100 105 {ECO:0000244|PDB:5WTE}.
HELIX 106 110 {ECO:0000244|PDB:5WTE}.
STRAND 111 115 {ECO:0000244|PDB:5WTE}.
HELIX 118 121 {ECO:0000244|PDB:5WTE}.
STRAND 124 137 {ECO:0000244|PDB:5WTE}.
STRAND 144 154 {ECO:0000244|PDB:5WTE}.
HELIX 162 166 {ECO:0000244|PDB:5WTE}.
STRAND 167 176 {ECO:0000244|PDB:5WTE}.
STRAND 178 184 {ECO:0000244|PDB:5WTE}.
STRAND 189 192 {ECO:0000244|PDB:5WTE}.
STRAND 195 197 {ECO:0000244|PDB:5WTE}.
STRAND 202 214 {ECO:0000244|PDB:5WTE}.
STRAND 217 219 {ECO:0000244|PDB:5WTE}.
STRAND 221 239 {ECO:0000244|PDB:5WTE}.
HELIX 265 268 {ECO:0000244|PDB:5WTE}.
STRAND 273 275 {ECO:0000244|PDB:5WTE}.
HELIX 276 278 {ECO:0000244|PDB:5WTE}.
HELIX 286 288 {ECO:0000244|PDB:5WTE}.
HELIX 297 300 {ECO:0000244|PDB:5WTE}.
STRAND 304 312 {ECO:0000244|PDB:5WTE}.
STRAND 322 325 {ECO:0000244|PDB:5WTE}.
TURN 336 339 {ECO:0000244|PDB:5WTE}.
HELIX 345 350 {ECO:0000244|PDB:5WTE}.
STRAND 353 366 {ECO:0000244|PDB:5WTE}.
STRAND 373 383 {ECO:0000244|PDB:5WTE}.
STRAND 385 387 {ECO:0000244|PDB:5WTE}.
HELIX 394 397 {ECO:0000244|PDB:5WTE}.
STRAND 402 410 {ECO:0000244|PDB:5WTE}.
STRAND 413 418 {ECO:0000244|PDB:5WTE}.
STRAND 423 425 {ECO:0000244|PDB:5WTE}.
STRAND 433 435 {ECO:0000244|PDB:5WTE}.
STRAND 444 456 {ECO:0000244|PDB:5WTE}.
STRAND 459 461 {ECO:0000244|PDB:5WTE}.
STRAND 463 481 {ECO:0000244|PDB:5WTE}.
STRAND 532 534 {ECO:0000244|PDB:5WTE}.
HELIX 540 542 {ECO:0000244|PDB:5WTE}.
TURN 549 553 {ECO:0000244|PDB:5WTE}.
STRAND 568 571 {ECO:0000244|PDB:5WTE}.
HELIX 576 579 {ECO:0000244|PDB:5WTE}.
STRAND 584 591 {ECO:0000244|PDB:5WTE}.
STRAND 593 603 {ECO:0000244|PDB:5WTE}.
STRAND 606 608 {ECO:0000244|PDB:5WTE}.
HELIX 616 621 {ECO:0000244|PDB:5WTE}.
TURN 622 624 {ECO:0000244|PDB:5WTE}.
STRAND 625 630 {ECO:0000244|PDB:5WTE}.
STRAND 632 640 {ECO:0000244|PDB:5WTE}.
STRAND 645 651 {ECO:0000244|PDB:5WTE}.
STRAND 662 664 {ECO:0000244|PDB:5WTE}.
HELIX 670 675 {ECO:0000244|PDB:5WTE}.
STRAND 679 682 {ECO:0000244|PDB:5WTE}.
TURN 683 685 {ECO:0000244|PDB:5WTE}.
STRAND 687 693 {ECO:0000244|PDB:5WTE}.
STRAND 698 700 {ECO:0000244|PDB:5WTE}.
HELIX 708 714 {ECO:0000244|PDB:5WTE}.
STRAND 716 725 {ECO:0000244|PDB:5WTE}.
STRAND 734 742 {ECO:0000244|PDB:5WTE}.
STRAND 747 751 {ECO:0000244|PDB:5WTE}.
STRAND 840 846 {ECO:0000244|PDB:4WZN}.
STRAND 850 853 {ECO:0000244|PDB:4WZN}.
STRAND 856 859 {ECO:0000244|PDB:4WZN}.
STRAND 861 872 {ECO:0000244|PDB:4WZN}.
STRAND 878 883 {ECO:0000244|PDB:4WZN}.
STRAND 886 893 {ECO:0000244|PDB:4WZN}.
STRAND 900 902 {ECO:0000244|PDB:4WZN}.
HELIX 905 914 {ECO:0000244|PDB:4WZN}.
HELIX 932 938 {ECO:0000244|PDB:4WZN}.
HELIX 947 957 {ECO:0000244|PDB:4WZN}.
STRAND 960 963 {ECO:0000244|PDB:4WZN}.
HELIX 964 968 {ECO:0000244|PDB:4WZN}.
HELIX 1521 1531 {ECO:0000244|PDB:2HAL}.
STRAND 1532 1539 {ECO:0000244|PDB:2HAL}.
STRAND 1545 1555 {ECO:0000244|PDB:2HAL}.
STRAND 1557 1561 {ECO:0000244|PDB:2HAL}.
HELIX 1562 1564 {ECO:0000244|PDB:2HAL}.
TURN 1565 1567 {ECO:0000244|PDB:2HAL}.
HELIX 1571 1573 {ECO:0000244|PDB:2HAL}.
STRAND 1574 1580 {ECO:0000244|PDB:2HAL}.
STRAND 1583 1588 {ECO:0000244|PDB:2HAL}.
HELIX 1589 1591 {ECO:0000244|PDB:2HAL}.
STRAND 1592 1595 {ECO:0000244|PDB:2HAL}.
STRAND 1597 1600 {ECO:0000244|PDB:2HAL}.
STRAND 1603 1608 {ECO:0000244|PDB:2HAL}.
HELIX 1619 1621 {ECO:0000244|PDB:2HAL}.
HELIX 1625 1630 {ECO:0000244|PDB:2HAL}.
TURN 1631 1633 {ECO:0000244|PDB:2HAL}.
STRAND 1636 1642 {ECO:0000244|PDB:2HAL}.
STRAND 1645 1651 {ECO:0000244|PDB:2HAL}.
STRAND 1655 1665 {ECO:0000244|PDB:2HAL}.
STRAND 1667 1669 {ECO:0000244|PDB:1HAV}.
STRAND 1671 1683 {ECO:0000244|PDB:2HAL}.
STRAND 1694 1698 {ECO:0000244|PDB:2HAL}.
HELIX 1700 1702 {ECO:0000244|PDB:2HAL}.
STRAND 1706 1714 {ECO:0000244|PDB:2HAL}.
STRAND 1717 1722 {ECO:0000244|PDB:2HAL}.
HELIX 1725 1730 {ECO:0000244|PDB:2HAL}.
SEQUENCE 2227 AA; 251508 MW; 01E225E7AEB740A6 CRC64;
MNMSRQGIFQ TVGSGLDHIL SLADIEEEQM IQSVDRTAVT GASYFTSVDQ SSVHTAEVGS
HQVEPLRTSV DKPGSKKTQG EKFFLIHSAD WLTTHALFHE VAKLDVVKLL YNEQFAVQGL
LRYHTYARFG IEIQVQINPT PFQQGGLICA MVPGDQSYGS IASLTVYPHG LLNCNINNVV
RIKVPFIYTR GAYHFKDPQY PVWELTIRVW SELNIGTGTS AYTSLNVLAR FTDLELHGLT
PLSTQMMRNE FRVSTTENVV NLSNYEDARA KMSFALDQED WKSDPSQGGG IKITHFTTWT
SIPTLAAQFP FNASDSVGQQ IKVIPVDPYF FQMTNTNPDQ KCITALASIC QMFCFWRGDL
VFDFQVFPTK YHSGRLLFCF VPGNELIDVS GITLKQATTA PCAVMDITGV QSTLRFRVPW
ISDTPYRVNR YTKSAHQKGE YTAIGKLIVY CYNRLTSPSN VASHVRVNVY LSAINLECFA
PLYHAMDVTT QVGDDSGGFS TTVSTEQNVP DPQVGITTMK DLKGKANRGK MDVSGVQAPV
GAITTIEDPV LAKKVPETFP ELKPGESRHT SDHMSIYKFM GRSHFLCTFT FNSNNKEYTF
PITLSSTSNP PHGLPSTLRW FFNLFQLYRG PLDLTIIITG ATDVDGMAWF TPVGLAVDTP
WVEKESALSI DYKTALGAVR FNTRRTGNIQ IRLPWYSYLY AVSGALDGLG DKTDSTFGLV
SIQIANYNHS DEYLSFSCYL SVTEQSEFYF PRAPLNSNAM LSTESMMSRI AAGDLESSVD
DPRSEEDKRF ESHIECRKPY KELRLEVGKQ RLKYAQEELS NEVLPPPRKM KGLFSQAKIS
LFYTEEHEIM KFSWRGVTAD TRALRRFGFS LAAGRSVWTL EMDAGVLTGR LIRLNDEKWT
EMKDDKIVSL IEKFTSNKYW SKVNFPHGML DLEEIAANSK DFPNMSETDL CFLLHWLNPK
KINLADRMLG LSGVQEIKEQ GVGLIAECRT FLDSIAGTLK SMMFGFHHSV TVEIINTVLC
FVKSGILLYV IQQLNQDEHS HIIGLLRVMN YADIGCSVIS CGKVFSKMLE TVFNWQMDSR
MMELRTQSFS NWLRDICSGI TIFKNFKDAI YWLYTKLKDF YEVNYGKKKD ILNILKDNQQ
KIEKAIEEAD EFCILQIQDV EKFEQYQKGV DLIQKLRTVH SMAQVDPNLM VHLSPLRDCI
ARVHQKLKNL GSINQAMVTR CEPVVCYLYG KRGGGKSLTS IALATKICKH YGVEPEKNIY
TKPVASDYWD GYSGQLVCII DDIGQNTTDE DWSDFCQLVS GCPMRLNMAS LEEKGRHFSS
PFIIATSNWS NPSPKTVYVK EAIDRRLHFK VEVKPASFFK NPHNDMLNVN LAKTNDAIKD
MSCVDLIMDG HNVSLMDLLS SLVMTVEIRK QNMTEFMELW SQGISDDDND SAVAEFFQSF
PSGEPSNSKL SGFFQSVTNH KWVAVGAAVG ILGVLVGGWF VYKHFSRKEE EPIPAEGVYH
GVTKPKQVIK LDADPVESQS TLEIAGLVRK NLVQFGVGEK NGCVRWVMNA LGVKDDWLLV
PSHAYKFEKD YEMMEFYFNR GGTYYSISAG NVVIQSLDVG FQDVVLMKVP TIPKFRDITQ
HFIKKGDVPR ALNRLATLVT TVNGTPMLIS EGPLKMEEKA TYVHKKNDGT TVDLTVDQAW
RGKGEGLPGM CGGALVSSNQ SIQNAILGIH VAGGNSILVA KLVTQEMFQN IDKKIESQRI
MKVEFTQCSM NVVSKTLFRK SPIYHHIDKT MINFPAAMPF SKAEIDPMAV MLSKYSLPIV
EEPEDYKEAS IFYQNKIVGK TQLVDDFLDL DMAITGAPGI DAINMDSSPG FPYVQEKLTK
RDLIWLDENG LLLGVHPRLA QRILFNTVMM ENCSDLDVVF TTCPKDELRP LEKVLESKTR
AIDACPLDYS ILCRMYWGPA ISYFHLNPGF HTGVAIGIDP DRQWDELFKT MIRFGDVGLD
LDFSAFDASL SPFMIREAGR IMSELSGTPS HFGTALINTI IYSKHLLYNC CYHVCGSMPS
GSPCTALLNS IINNVNLYYV FSKIFGKSPV FFCQALKILC YGDDVLIVFS RDVQIDNLDL
IGQKIVDEFK KLGMTATSAD KNVPQLKPVS ELTFLKRSFN LVEDRIRPAI SEKTIWSLIA
WQRSNAEFEQ NLENAQWFAF MHGYEFYQKF YYFVQSCLEK EMIEYRLKSY DWWRMRFYDQ
CFICDLS


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18-003-43690 Guanine nucleotide-binding protein subunit beta-like protein 1 - G protein subunit beta-like protein 1; WD40 repeat-containing protein deleted in VCFS; Protein WDVCF; WD repeat-containing protein 14; 0.1 mg Protein A
U1773h CLIA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
E1773h ELISA kit G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB32247 ADP-ribosylation factor-like protein 6-interacting protein 5,Aip-5,ARL-6-interacting protein 5,ARL6IP5,Cytoskeleton-related vitamin A-responsive protein,Dermal papilla-derived protein 11,DERP11,Glutam
E1773h ELISA G-CSF-induced gene 1 protein,GIG1,GIG-1 protein,GMP-17,Granule membrane protein of 17 kDa,Homo sapiens,Human,Natural killer cell protein 7,NKG7,p15-TIA-1,Protein NKG7 96T
EIAAB31034 Androgen receptor-interacting protein 3,ARIP3,DAB2-interacting protein,DIP,E3 SUMO-protein ligase PIAS2,Homo sapiens,Human,Miz1,Msx-interacting zinc finger protein,PIAS2,PIAS-NY protein,PIASX,Protein
EIAAB29586 Mouse,Mus musculus,p53-induced gene 11 protein,Pig11,Tp53i11,Transformation related protein 53 inducible protein 11,Trp53i11,Tumor protein p53-inducible protein 11
EIAAB43486 Mouse,Mus musculus,Protein TAP1,Protein TRUSS,Rabex-5_Rin2-interacting protein,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.01 mg
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.002 mg
EIAAB43485 C20orf188,Homo sapiens,Human,Protein TAP1,Protein TRUSS,Short transient receptor potential channel 4-associated protein,TNF-receptor ubiquitous scaffolding_signaling protein,Trp4-associated protein,TR
EIAAB38162 Homo sapiens,Human,MAP,Merlin-associated protein,RabGAPLP,RABGAPLP,Rab-GTPase-activating protein-like protein,RUN and TBC1 domain-containing protein 3,RUTBC3,SGSM3,Small G protein signaling modulator
10-663-45493 Heat Shock Protein 22kD (HSP22) Human - HspB8; Alpha crystallin C chain; Small stress protein-like protein HSP22; E2-induced gene 1 protein; Protein kinase H11 N_A 0.1 mg
EIAAB33912 E3 ubiquitin-protein ligase RBBP6,Mouse,Mus musculus,P2pr,p53-associated cellular protein of testis,Pact,Proliferation potential-related protein,Protein P2P-R,Rbbp6,Retinoblastoma-binding protein 6


 

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